Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.
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Autoactivation of Thrombin PrecursorsSuppression of hepatic hepcidin expression in response to acute iron deprivation is associated with an increase of matriptase-2 proteinN-glycosylation is required for matriptase-2 autoactivation and ectodomain sheddingCleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide librariesEctodomain shedding and autocleavage of the cardiac membrane protease corin.Low intracellular iron increases the stability of matriptase-2.Regulation of TMPRSS6 by BMP6 and iron in human cells and mice.Corin in clinical laboratory diagnostics3,1-Benzothiazines, 1,4-Benzodioxines and 1,4-Benzoxazines as Inhibitors of Matriptase-2: Outcome of a Focused Screening Approach.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Iron refractory iron deficiency anemiaMembrane-anchored serine proteases in health and disease.Histone H4 promotes prothrombin autoactivation.Control of systemic iron homeostasis by the hemojuvelin-hepcidin axis.Essential role of endocytosis of the type II transmembrane serine protease TMPRSS6 in regulating its functionality.En Route to New Therapeutic Options for Iron Overload Diseases: Matriptase-2 as a Target for Kunitz-Type Inhibitors.Limiting the Number of Potential Binding Modes by Introducing Symmetry into Ligands: Structure-Based Design of Inhibitors for Trypsin-Like Serine Proteases.Proprotein convertase PC7 enhances the activation of the EGF receptor pathway through processing of the EGF precursor.Inactive matriptase-2 mutants found in IRIDA patients still repress hepcidin in a transfection assay despite having lost their serine protease activity.Functional analysis of corin protein domains required for PCSK6-mediated activation.Transcriptome analysis reveals TMPRSS6 isoforms with distinct functionalities.Phosphono Bisbenzguanidines as Irreversible Dipeptidomimetic Inhibitors and Activity-Based Probes of Matriptase-2.Interplay between conformational selection and zymogen activation.A Short Peptide Inhibitor as an Activity-Based Probe for Matriptase-2.
P2860
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P2860
Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.
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2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-my
2010年学术文章
@zh-sg
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name
Proteolytic processing of the ...... release from the cell surface.
@en
Proteolytic processing of the ...... release from the cell surface.
@nl
type
label
Proteolytic processing of the ...... release from the cell surface.
@en
Proteolytic processing of the ...... release from the cell surface.
@nl
prefLabel
Proteolytic processing of the ...... release from the cell surface.
@en
Proteolytic processing of the ...... release from the cell surface.
@nl
P2093
P2860
P356
P1433
P1476
Proteolytic processing of the ...... release from the cell surface.
@en
P2093
Andreas Janzer
Angelika Horstmeyer
Eva Maurer
Jochen Walter
Kai Prager
Katharina Arenz
Marit Stirnberg
Michael Gütschow
Patrick Wunderlich
Sonja Kolp
P2860
P356
10.1042/BJ20091565
P407
P577
2010-08-01T00:00:00Z